Related Experiment Video
Updated: Jul 16, 2026
How to Study Basement Membrane Stiffness as a Biophysical Trigger in Prostate Cancer and Other Age-related Pathologies or Metabolic Diseases
Published on: September 20, 2016
[Stress proteins in prostate cancer. Challenge and promise]
B A Hadaschik1, S W Melchior, R D Sowery
1The Prostate Centre at Vancouver General Hospital, 2660 Oak Street, V6H 3Z6 Vancouver. boris.hadaschik@vch.ca
Abstract:
Therapeutic resistance is the underlying basis for most cancer deaths. Exposure to anticancer therapies induces expression of many stress proteins, including heat shock proteins and clusterin. These molecular chaperones interact with various client proteins to assist in their folding and enhance cellular recovery from stress conditions. Cellular stress and cell death are linked, as the induction of chaperones appear to function at key regulatory points in the control of apoptosis. On this basis and on the role of stress proteins in the regulation of steroid receptors, kinases, caspases, and other protein remodeling events, it is not surprising that molecular chaperones have been implicated in resistance to anticancer treatments. Recently, several chaperones have been reported to be involved in development and progression of hormone-refractory prostate cancer. In this review, we address some of the events initiated by treatment-induced stress and discuss the potential role of chaperone inhibitors in prostate cancer treatment.
Insights
Therapeutic resistance in cancer is linked to stress proteins like heat shock proteins and clusterin. Inhibiting these molecular chaperones may offer a new strategy for treating hormone-refractory prostate cancer.
Area of Science:
- Molecular biology
- Oncology
- Biochemistry
Context:
- Therapeutic resistance is a major cause of cancer mortality.
- Anticancer therapies trigger cellular stress responses, inducing molecular chaperones.
- Prostate cancer, particularly hormone-refractory forms, shows chaperone involvement.
Purpose:
- To review the role of molecular chaperones in therapeutic resistance.
- To explore the link between stress proteins and cancer progression.
- To discuss chaperone inhibitors as a potential prostate cancer treatment.
Summary:
- Molecular chaperones, including heat shock proteins and clusterin, are upregulated by anticancer treatments.
- These proteins aid in client protein folding and cellular recovery from stress, influencing apoptosis.
- Chaperones are implicated in resistance to cancer therapies and the progression of hormone-refractory prostate cancer.
Impact:
- Understanding chaperone function in resistance can lead to novel therapeutic strategies.
- Chaperone inhibitors represent a promising avenue for overcoming treatment resistance in prostate cancer.
- This review highlights the potential of targeting molecular chaperones to improve cancer patient outcomes.
